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Rif1 promotes association of G-quadruplex (G4) by its specific G4 binding and oligomerization activities
Rif1 is a conserved protein regulating replication timing and binds preferentially to the vicinity of late-firing/dormant origins in fission yeast. The Rif1 binding sites on the fission yeast genome have an intrinsic potential to generate G-quadruplex (G4) structures to which purified Rif1 preferent...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6565636/ https://www.ncbi.nlm.nih.gov/pubmed/31197198 http://dx.doi.org/10.1038/s41598-019-44736-9 |
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author | Masai, Hisao Fukatsu, Rino Kakusho, Naoko Kanoh, Yutaka Moriyama, Kenji Ma, Yue Iida, Keisuke Nagasawa, Kazuo |
author_facet | Masai, Hisao Fukatsu, Rino Kakusho, Naoko Kanoh, Yutaka Moriyama, Kenji Ma, Yue Iida, Keisuke Nagasawa, Kazuo |
author_sort | Masai, Hisao |
collection | PubMed |
description | Rif1 is a conserved protein regulating replication timing and binds preferentially to the vicinity of late-firing/dormant origins in fission yeast. The Rif1 binding sites on the fission yeast genome have an intrinsic potential to generate G-quadruplex (G4) structures to which purified Rif1 preferentially binds. We previously proposed that Rif1 generates chromatin architecture that may determine replication timing by facilitating the chromatin loop formation. Here, we conducted detailed biochemical analyses on Rif1 and its G4 binding. Rif1 prefers sequences containing long stretches of guanines and binds preferentially to the multimeric G4 of parallel or hybrid/mix topology. Rif1 forms oligomers and binds simultaneously to multiple G4. We present a model on how Rif1 may facilitate the formation of chromatin architecture through its G4 binding and oligomerization properties. |
format | Online Article Text |
id | pubmed-6565636 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-65656362019-06-20 Rif1 promotes association of G-quadruplex (G4) by its specific G4 binding and oligomerization activities Masai, Hisao Fukatsu, Rino Kakusho, Naoko Kanoh, Yutaka Moriyama, Kenji Ma, Yue Iida, Keisuke Nagasawa, Kazuo Sci Rep Article Rif1 is a conserved protein regulating replication timing and binds preferentially to the vicinity of late-firing/dormant origins in fission yeast. The Rif1 binding sites on the fission yeast genome have an intrinsic potential to generate G-quadruplex (G4) structures to which purified Rif1 preferentially binds. We previously proposed that Rif1 generates chromatin architecture that may determine replication timing by facilitating the chromatin loop formation. Here, we conducted detailed biochemical analyses on Rif1 and its G4 binding. Rif1 prefers sequences containing long stretches of guanines and binds preferentially to the multimeric G4 of parallel or hybrid/mix topology. Rif1 forms oligomers and binds simultaneously to multiple G4. We present a model on how Rif1 may facilitate the formation of chromatin architecture through its G4 binding and oligomerization properties. Nature Publishing Group UK 2019-06-13 /pmc/articles/PMC6565636/ /pubmed/31197198 http://dx.doi.org/10.1038/s41598-019-44736-9 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Masai, Hisao Fukatsu, Rino Kakusho, Naoko Kanoh, Yutaka Moriyama, Kenji Ma, Yue Iida, Keisuke Nagasawa, Kazuo Rif1 promotes association of G-quadruplex (G4) by its specific G4 binding and oligomerization activities |
title | Rif1 promotes association of G-quadruplex (G4) by its specific G4 binding and oligomerization activities |
title_full | Rif1 promotes association of G-quadruplex (G4) by its specific G4 binding and oligomerization activities |
title_fullStr | Rif1 promotes association of G-quadruplex (G4) by its specific G4 binding and oligomerization activities |
title_full_unstemmed | Rif1 promotes association of G-quadruplex (G4) by its specific G4 binding and oligomerization activities |
title_short | Rif1 promotes association of G-quadruplex (G4) by its specific G4 binding and oligomerization activities |
title_sort | rif1 promotes association of g-quadruplex (g4) by its specific g4 binding and oligomerization activities |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6565636/ https://www.ncbi.nlm.nih.gov/pubmed/31197198 http://dx.doi.org/10.1038/s41598-019-44736-9 |
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